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  1. Article ; Online: Anchored protein kinase A signalling in cardiac cellular electrophysiology.

    Soni, Siddarth / Scholten, Arjen / Vos, Marc A / van Veen, Toon A B

    Journal of cellular and molecular medicine

    2014  Volume 18, Issue 11, Page(s) 2135–2146

    Abstract: The cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) is an elementary molecule involved in both acute and chronic modulation of cardiac function. Substantial research in recent years has highlighted the importance of A-kinase ... ...

    Abstract The cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) is an elementary molecule involved in both acute and chronic modulation of cardiac function. Substantial research in recent years has highlighted the importance of A-kinase anchoring proteins (AKAP) therein as they act as the backbones of major macromolecular signalling complexes of the β-adrenergic/cAMP/PKA pathway. This review discusses the role of AKAP-associated protein complexes in acute and chronic cardiac modulation by dissecting their role in altering the activity of different ion channels, which underlie cardiac action potential (AP) generation. In addition, we review the involvement of different AKAP complexes in mechanisms of cardiac remodelling and arrhythmias.
    MeSH term(s) A Kinase Anchor Proteins/metabolism ; Action Potentials ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Electrophysiology ; Heart/physiopathology ; Humans ; Ion Channels/metabolism ; Myocardium/enzymology ; Myocardium/metabolism ; Signal Transduction ; beta-Adrenergic Receptor Kinases/metabolism
    Chemical Substances A Kinase Anchor Proteins ; Ion Channels ; Cyclic AMP (E0399OZS9N) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; beta-Adrenergic Receptor Kinases (EC 2.7.11.15)
    Language English
    Publishing date 2014-09-12
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2074559-X
    ISSN 1582-4934 ; 1582-4934 ; 1582-1838
    ISSN (online) 1582-4934
    ISSN 1582-4934 ; 1582-1838
    DOI 10.1111/jcmm.12365
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5752: Show issues Location:
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  2. Article ; Online: A Proteomics Approach to Identify New Putative Cardiac Intercalated Disk Proteins.

    Soni, Siddarth / Raaijmakers, Antonia J A / Raaijmakers, Linsey M / Damen, J Mirjam A / van Stuijvenberg, Leonie / Vos, Marc A / Heck, Albert J R / van Veen, Toon A B / Scholten, Arjen

    PloS one

    2016  Volume 11, Issue 5, Page(s) e0152231

    Abstract: Aims: Synchronous beating of the heart is dependent on the efficient functioning of the cardiac intercalated disk (ID). The ID is composed of a complex protein network enabling electrical continuity and chemical communication between individual ... ...

    Abstract Aims: Synchronous beating of the heart is dependent on the efficient functioning of the cardiac intercalated disk (ID). The ID is composed of a complex protein network enabling electrical continuity and chemical communication between individual cardiomyocytes. Recently, several different studies have shed light on increasingly prevalent cardiac diseases involving the ID. Insufficient knowledge of its composition makes it difficult to study these disease mechanisms in more detail and therefore here we aim expand the ID proteome. Here, using a combination of general membrane enrichment, in-depth quantitative proteomics and an intracellular location driven bioinformatics approach, we aim to discover new putative ID proteins in rat ventricular tissue.
    Methods and results: General membrane isolation, enriched amongst others also with ID proteins as based on presence of the established markers connexin-43 and n-cadherin, was performed using centrifugation. By mass spectrometry, we quantitatively evaluated the level of 3455 proteins in the enriched membrane fraction (EMF) and its counterpart, the soluble cytoplasmic fraction. These data were stringently filtered to generate a final set of 97 enriched, putative ID proteins. These included Cx43 and n-cadherin, but also many interesting novel candidates. We selected 4 candidates (Flotillin-2 (FLOT2), Nexilin (NEXN), Popeye-domain-containg-protein 2 (POPDC2) and thioredoxin-related-transmembrane-protein 2 (TMX2)) and confirmed their co-localization with n-cadherin in the ID of human and rat heart cryo-sections, and isolated dog cardiomyocytes.
    Conclusion: The presented proteomics dataset of putative new ID proteins is a valuable resource for future research into this important molecular intersection of the heart.
    MeSH term(s) Animals ; Gap Junctions/metabolism ; Humans ; Male ; Membrane Proteins/metabolism ; Myocardium/metabolism ; Proteomics ; Rats ; Rats, Wistar
    Chemical Substances Membrane Proteins ; flotillins
    Language English
    Publishing date 2016-05-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0152231
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Neuronal nitric oxide synthase-dependent amelioration of diastolic dysfunction in rats with chronic renocardiac syndrome.

    Bongartz, Lennart G / Soni, Siddarth / Cramer, Maarten-Jan / Steendijk, Paul / Gaillard, Carlo A J M / Verhaar, Marianne C / Doevendans, Pieter A / van Veen, Toon A / Joles, Jaap A / Braam, Branko

    Cardiorenal medicine

    2015  Volume 5, Issue 1, Page(s) 69–78

    Abstract: We have recently described the chronic renocardiac syndrome (CRCS) in rats with renal failure, cardiac dysfunction and low nitric oxide (NO) availability by combining subtotal nephrectomy and transient low-dose NO synthase (NOS) inhibition. Cardiac gene ... ...

    Abstract We have recently described the chronic renocardiac syndrome (CRCS) in rats with renal failure, cardiac dysfunction and low nitric oxide (NO) availability by combining subtotal nephrectomy and transient low-dose NO synthase (NOS) inhibition. Cardiac gene expression of the neuronal isoform of NOS (nNOS) was induced. Hence, we studied the role of nNOS, in vivo cardiac function and β-adrenergic response in our CRCS model by micromanometer/conductance catheter. Left ventricular (LV) hemodynamics were studied during administration of dobutamine (dobu), the highly specific irreversible inhibitor of nNOS L-VNIO [L-N5-(1-Imino-3-butenyl)-ornithine], or both at steady state and during preload reduction. Rats with CRCS showed LV systolic dysfunction at baseline, together with prolonged diastolic relaxation and rightward shift of the end-systolic pressure-volume relationships. After L-VNIO infusion, diastolic relaxation of CRCS rats further prolonged. The time constant of active relaxation (tau) increased by 25 ± 6% from baseline (p < 0.05), and the maximal rate of pressure decrease was 36 ± 7% slower (p < 0.001). These variables did not change in controls. In our CRCS model, nNOS did not seem to affect systolic dysfunction. In summary, in this model of CRCS, blockade of nNOS further worsens diastolic dysfunction and L-VNIO does not influence inherent contractility and the response to dobu stress.
    Language English
    Publishing date 2015-02
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2595659-0
    ISSN 1664-5502 ; 1664-3828
    ISSN (online) 1664-5502
    ISSN 1664-3828
    DOI 10.1159/000370052
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Reorganized PKA-AKAP associations in the failing human heart.

    Aye, Thin-Thin / Soni, Siddarth / van Veen, Toon A B / van der Heyden, Marcel A G / Cappadona, Salvatore / Varro, Andras / de Weger, Roel A / de Jonge, Nicolaas / Vos, Marc A / Heck, Albert J R / Scholten, Arjen

    Journal of molecular and cellular cardiology

    2012  Volume 52, Issue 2, Page(s) 511–518

    Abstract: Here we reveal that the characterization of large-scale re-arrangements of signaling scaffolds induced by heart failure can serve as a novel concept to identify more specific therapeutic targets. In the mammalian heart, the cAMP pathway, with the cAMP- ... ...

    Abstract Here we reveal that the characterization of large-scale re-arrangements of signaling scaffolds induced by heart failure can serve as a novel concept to identify more specific therapeutic targets. In the mammalian heart, the cAMP pathway, with the cAMP-dependent protein kinase (PKA) in a central role, acts directly downstream of adrenergic receptors to mediate cardiac contractility and rhythm. Heart failure, characterized by severe alterations in adrenergic stimulation is, amongst other interventions, often treated with β-blockers. Contrasting results, however, have shown both beneficial and detrimental effects of decreased cAMP levels in failing hearts. We hypothesize that the origin of this behavior lies in the complex spatiotemporal organization of the regulatory subunit of PKA (PKA-R), which associates tightly with various A-kinase anchoring proteins (AKAPs) to specifically localize PKA's activity. Using chemical proteomics directly applied to human patient and control heart tissue we demonstrate that the association profile of PKA-R with several AKAPs is severely altered in the failing heart, for instance effecting the interaction between PKA and the novel AKAP SPHKAP was 6-fold upregulated upon failing heart conditions. Also a significant increase in captured cGMP-dependent protein kinase (PKG) and phosphodiesterase 2 (PDE2) was observed. The observed altered profiles can already explain many aspects of the aberrant cAMP-response in the failing human heart, validating that this dataset may provide a resource for several novel, more specific, treatment options. This article is part of a Special Issue entitled "Local Signaling in Myocytes".
    MeSH term(s) A Kinase Anchor Proteins/metabolism ; Adult ; Aged ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Female ; Heart Failure/metabolism ; Humans ; Male ; Middle Aged ; Myocardium/metabolism ; Myofibrils/metabolism ; Protein Binding ; Protein Interaction Mapping ; Proteome/metabolism ; Signal Transduction ; Young Adult
    Chemical Substances A Kinase Anchor Proteins ; Proteome ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
    Language English
    Publishing date 2012-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80157-4
    ISSN 1095-8584 ; 0022-2828
    ISSN (online) 1095-8584
    ISSN 0022-2828
    DOI 10.1016/j.yjmcc.2011.06.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 426: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  5. Article: Neuronal Nitric Oxide Synthase-Dependent Amelioration of Diastolic Dysfunction in Rats with Chronic Renocardiac Syndrome

    Bongartz, Lennart G. / Soni, Siddarth / Cramer, Maarten-Jan / Steendijk, Paul / Gaillard, Carlo A.J.M. / Verhaar, Marianne C. / Doevendans, Pieter A. / van Veen, Toon A. / Joles, Jaap A. / Braam, Branko

    Cardiorenal Medicine

    2015  Volume 5, Issue 1, Page(s) 69–78

    Abstract: We have recently described the chronic renocardiac syndrome (CRCS) in rats with renal failure, cardiac dysfunction and low nitric oxide (NO) availability by combining subtotal nephrectomy and transient low-dose NO synthase (NOS) inhibition. Cardiac gene ... ...

    Institution Departments of Nephrology Cardiology, and Medical Physiology, University Medical Center Utrecht, Utrecht Department of Cardiology and Cardiothoracic Surgery, Leiden University Medical Center, Leiden, and Department of Nephrology, University Medical Center Groningen, Groningen, The Netherlands Division of Nephrology and Immunology, Department of Medicine and Department Physiology, University of Alberta, Edmonton, Alta., Canada
    Abstract We have recently described the chronic renocardiac syndrome (CRCS) in rats with renal failure, cardiac dysfunction and low nitric oxide (NO) availability by combining subtotal nephrectomy and transient low-dose NO synthase (NOS) inhibition. Cardiac gene expression of the neuronal isoform of NOS (nNOS) was induced. Hence, we studied the role of nNOS, in vivo cardiac function and β-adrenergic response in our CRCS model by micromanometer/conductance catheter. Left ventricular (LV) hemodynamics were studied during administration of dobutamine (dobu), the highly specific irreversible inhibitor of nNOS L-VNIO [L-N5-(1-Imino-3-butenyl)-ornithine], or both at steady state and during preload reduction. Rats with CRCS showed LV systolic dysfunction at baseline, together with prolonged diastolic relaxation and rightward shift of the end-systolic pressure-volume relationships. After L-VNIO infusion, diastolic relaxation of CRCS rats further prolonged. The time constant of active relaxation (tau) increased by 25 ± 6% from baseline (p < 0.05), and the maximal rate of pressure decrease was 36 ± 7% slower (p < 0.001). These variables did not change in controls. In our CRCS model, nNOS did not seem to affect systolic dysfunction. In summary, in this model of CRCS, blockade of nNOS further worsens diastolic dysfunction and L-VNIO does not influence inherent contractility and the response to dobu stress.
    Keywords Diastolic function ; Cardiorenal syndrome ; Neuronal nitric oxide synthase
    Language English
    Publishing date 2015-01-16
    Publisher S. Karger AG
    Publishing place Basel, Switzerland
    Document type Article
    Note Original Paper
    ZDB-ID 2595659-0
    ISSN 1664-5502 ; 1664-3828
    ISSN (online) 1664-5502
    ISSN 1664-3828
    DOI 10.1159/000370052
    Database Karger publisher's database

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  6. Article ; Online: Oxidized CaMKII causes cardiac sinus node dysfunction in mice.

    Swaminathan, Paari Dominic / Purohit, Anil / Soni, Siddarth / Voigt, Niels / Singh, Madhu V / Glukhov, Alexey V / Gao, Zhan / He, B Julie / Luczak, Elizabeth D / Joiner, Mei-ling A / Kutschke, William / Yang, Jinying / Donahue, J Kevin / Weiss, Robert M / Grumbach, Isabella M / Ogawa, Masahiro / Chen, Peng-Sheng / Efimov, Igor / Dobrev, Dobromir /
    Mohler, Peter J / Hund, Thomas J / Anderson, Mark E

    The Journal of clinical investigation

    2011  Volume 121, Issue 8, Page(s) 3277–3288

    Abstract: Sinus node dysfunction (SND) is a major public health problem that is associated with sudden cardiac death and requires surgical implantation of artificial pacemakers. However, little is known about the molecular and cellular mechanisms that cause SND. ... ...

    Abstract Sinus node dysfunction (SND) is a major public health problem that is associated with sudden cardiac death and requires surgical implantation of artificial pacemakers. However, little is known about the molecular and cellular mechanisms that cause SND. Most SND occurs in the setting of heart failure and hypertension, conditions that are marked by elevated circulating angiotensin II (Ang II) and increased oxidant stress. Here, we show that oxidized calmodulin kinase II (ox-CaMKII) is a biomarker for SND in patients and dogs and a disease determinant in mice. In wild-type mice, Ang II infusion caused sinoatrial nodal (SAN) cell oxidation by activating NADPH oxidase, leading to increased ox-CaMKII, SAN cell apoptosis, and SND. p47-/- mice lacking functional NADPH oxidase and mice with myocardial or SAN-targeted CaMKII inhibition were highly resistant to SAN apoptosis and SND, suggesting that ox-CaMKII-triggered SAN cell death contributed to SND. We developed a computational model of the sinoatrial node that showed that a loss of SAN cells below a critical threshold caused SND by preventing normal impulse formation and propagation. These data provide novel molecular and mechanistic information to understand SND and suggest that targeted CaMKII inhibition may be useful for preventing SND in high-risk patients.
    MeSH term(s) Angiotensin II/metabolism ; Animals ; Apoptosis ; Biomarkers/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism ; Dogs ; Electrocardiography/methods ; Humans ; Mice ; Mice, Transgenic ; NADPH Oxidases/genetics ; Oxygen/chemistry ; Reactive Oxygen Species ; Sick Sinus Syndrome/genetics ; Sick Sinus Syndrome/metabolism ; Sinoatrial Node/pathology
    Chemical Substances Biomarkers ; Reactive Oxygen Species ; Angiotensin II (11128-99-7) ; NADPH Oxidases (EC 1.6.3.-) ; neutrophil cytosolic factor 1 (EC 1.6.3.1) ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 (EC 2.7.11.17) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2011-07-25
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 3067-3
    ISSN 1558-8238 ; 0021-9738
    ISSN (online) 1558-8238
    ISSN 0021-9738
    DOI 10.1172/JCI57833
    Database MEDical Literature Analysis and Retrieval System OnLINE

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